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Updated: Feb 5, 2026
08:53
Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species
Published on: May 7, 2018
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Protein probes to visualize sphingomyelin and ceramide phosphoethanolamine
Françoise Hullin-Matsuda1, Motohide Murate2, Toshihide Kobayashi2
1Univ-Lyon, CarMeN Laboratory, Inserm U1060, INRA U1397, Université Claude Bernard Lyon 1, INSA Lyon, 69621, Villeurbanne, France.
Chemistry and Physics of Lipids
|September 9, 2018
Summary
Specific proteins can visualize sphingomyelin (SM) and ceramide phosphoethanolamine (CPE) in cells. These probes, derived from toxins or similar structures, offer insights into lipid detection and membrane organization.
Area of Science:
- Biochemistry
- Cell Biology
- Biophysics
Background:
- Sphingomyelin (SM) is a key sphingolipid in mammals, while ceramide phosphoethanolamine (CPE) is abundant in invertebrates.
- Visualizing endogenous SM and CPE requires probes that recognize their specific chemical structures.
Purpose of the Study:
- To review proteins that specifically bind SM and CPE.
- To discuss the applications and limitations of these lipid-binding proteins as cellular probes.
Main Methods:
- Literature review of known SM- and CPE-binding proteins.
- Analysis of protein characteristics, including specificity and binding constants.
- Examination of protein labeling techniques (fluorophores, fluorescent proteins, etc.).
Main Results:
- Several proteins, including lysenin, equinatoxin II, pleurotolysin A2, ostreolysin, erylysin A, and nakanori, exhibit specific binding to SM, CPE, or cholesterol-rich membranes.
- These proteins, often derived from toxins, can be labeled for detection but have limitations related to specificity and membrane lipid organization.
Conclusions:
- Specific SM- and CPE-binding proteins serve as valuable tools for visualizing these lipids in cellular contexts.
- Understanding their binding properties and limitations is crucial for accurate interpretation of experimental results.
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